Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

2OZX

Solution structure of human phosphohistidine phosphatase 1 in phosphate free form

Functional Information from GO Data
ChainGOidnamespacecontents
A0004721molecular_functionphosphoprotein phosphatase activity
A0004857molecular_functionenzyme inhibitor activity
A0005515molecular_functionprotein binding
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0016604cellular_componentnuclear body
A0016787molecular_functionhydrolase activity
A0019855molecular_functioncalcium channel inhibitor activity
A0030036biological_processactin cytoskeleton organization
A0035774biological_processpositive regulation of insulin secretion involved in cellular response to glucose stimulus
A0044325molecular_functiontransmembrane transporter binding
A0050860biological_processnegative regulation of T cell receptor signaling pathway
A0051015molecular_functionactin filament binding
A0061851cellular_componentleading edge of lamellipodium
A0070062cellular_componentextracellular exosome
A0097581biological_processlamellipodium organization
A0101006molecular_functionprotein histidine phosphatase activity
A2000147biological_processpositive regulation of cell motility
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"18991813","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18991813","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"N-acetylalanine","evidences":[{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22223895","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues6
DetailsM-CSA 952
ChainResidueDetails
ALYS21electrostatic stabiliser, modifies pKa
AHIS53proton acceptor, proton donor
AALA54electrostatic stabiliser
AARG78electrostatic stabiliser
ASER94electrostatic stabiliser
AALA96electrostatic stabiliser

243083

PDB entries from 2025-10-15

PDB statisticsPDBj update infoContact PDBjnumon